CATH Classification

Domain Context

CATH Clusters

Superfamily Kinase associated domain 1, KA1
Functional Family Non-specific serine/threonine protein kinase

Enzyme Information
[Tau protein] kinase.
based on mapping to UniProt P54645
ATP + [tau protein] = ADP + [tau protein] phosphate.
-!- Activated by tubulin. -!- Involved in the formation of paired helical filaments, which are the main fibrous component of all fibrillary lesions in brain and are associated with Alzheimer's disease. -!- Formerly EC
[Hydroxymethylglutaryl-CoA reductase (NADPH)] kinase.
based on mapping to UniProt P54645
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate.
-!- Activated by AMP. -!- EC is inactivated by the phosphorylation of the enzyme protein. -!- Histones can also act as acceptors. -!- Can also phosphorylate EC and EC -!- Thr-172 within the catalytic subunit (alpha-subunit) is the major site phosphorylated by the AMP-activated protein kinase kinase. -!- GTP can act instead of ATP. -!- Formerly EC
[Acetyl-CoA carboxylase] kinase.
based on mapping to UniProt P54645
ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate.
-!- Phosphorylates and inactivates EC, which can be dephosphorylated and reactivated by EC -!- More active toward the dimeric form of acetyl-CoA carboxylase than the polymeric form. -!- Phosphorylates serine residues. -!- Formerly EC and EC
Non-specific serine/threonine protein kinase.
based on mapping to UniProt P54645
ATP + a protein = ADP + a phosphoprotein.
-!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC and EC

UniProtKB Entries (1)

Rattus norvegicus
5'-AMP-activated protein kinase subunit gamma-1

PDB Structure

External Links
Primary Citation
AMP-activated protein kinase undergoes nucleotide-dependent conformational changes
Chen, L., Wang, J., Zhang, Y.-Y., Yan, S.F., Neumann, D., Schlattner, U., Wang, Z.-X., Wu, J.-W.